The 160k α1(IV) Chain, a Short Form of a Type IV Collagen Polypeptide, of Bovine Lens Capsule Retains the NC1 Domain

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  • IWATA Masao
    Departmnet of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo
  • SADO Yoshikazu
    Division of Immunology, Shigei Medical Research Institute
  • SASAKI Tasuku
    Departmnet of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo
  • IMAMURA Yasutada
    Departmnet of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo
  • NINOMIYA Yoshifumi
    Department of Molecular Biology and Biochemistry, Okayama University Medical School
  • HAYASHI Toshihiko
    Departmnet of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo

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We recently reported that the bovine lens capsule contained a shorter α1(IV) chain (160 k) as a major polypeptide in addition to the 180 k α1(IV) chain [J. Biochem. (1995) 117, 1298-1304]. Two experiments were performed to examine whether or not the 160 k polypeptide retained the carboxyl-terminal NC1 domain. On immunoblotting analysis with a monoclonal antibody (H11) raised against the NC1 domain of the human α1(IV) chain [positions 1643-1650; near the carboxyl-terminal end of the human α1(IV) chain], the 180 k and 160 k polypeptides showed identical immunoreactivity, suggesting that the two chains had the same human α1(IV) collagen NC1 domain sequence. Another monoclonal antibody (H21) specific for the NC1 domain of human α2(IV) did not react with these polypeptides, but with the bands corresponding to 175 k and 155 k. The 160 k polypeptide was selectively solubilized from bovine lens capsules, leaving the other major polypeptides, 180 k and 175 k, insoluble. The 160 k polypeptide was separated by preparative electrophoresis. Bacterial collagenase digestion of the separated 160 k polypeptide produced collagenase-resistant segments of about 29 k and 30 k in size based on globular standards. These sizes corresponded well with those of the NC1 domains of type IV collagen α chains (25-30 k). The results indicated that the 160 k polypeptide retained the carboxyl-terminal NC1 domain of the α1(IV) chain. In turn, the 20 k polypeptide of the amino-terminal region or the 7 S domain of 180 k α1(IV) would have been excised to yield 160 k α1(IV), assuming that the 160 k α1(IV) chain is a processed form of the 180 k α1(IV) one and not an alternatively spliced chain of the α1(IV) gene.

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